@article {von Meyerinck700, author = {L von Meyerinck and B L Coffman and M D Green and R B Kirkpatrick and A Schmoldt and T R Tephly}, title = {Separation, purification, and characterization of digitoxigenin-monodigitoxoside UDP-glucuronosyltransferase activity.}, volume = {13}, number = {6}, pages = {700--704}, year = {1985}, publisher = {American Society for Pharmacology and Experimental Therapeutics}, abstract = {Glucuronidation of digitoxigenin-monodigitoxoside was investigated in liver microsomes from spironolactone-induced male Wistar rats. Isolation of a specific digitoxigenin-monodigitoxoside UDP-glucuronosyltransferase was possible utilizing chromatofocusing chromatography with a gradient from pH 10.1 to 8.0 after solubilizing the microsomal protein with the nonionic detergent Emulgen 911. The digitoxigenin-monodigitoxoside UDP-glucuronosyltransferase was further purified using UDP-hexanolamine Sepharose 4B affinity chromatography. The highly purified (75-fold) enzyme showed activity toward digitoxigenin-monodigitoxoside and slight activity toward digitoxigenin-bisdigitoxoside, whereas digitoxin and substrates for p-nitrophenol, 17 beta-OH steroid, and 3 alpha-OH steroid UDP-glucuronosyltransferases were not glucuronidated. In addition, bilirubin, morphine, estrone, 4-hydroxybiphenyl, and aromatic amines were not glucuronidated by this protein. These results strongly confirm the presence of a form of UDP-glucuronosyltransferase, which is highly specific for the glucuronidation of digitoxigenin-monodigitoxoside.}, issn = {0090-9556}, URL = {https://dmd.aspetjournals.org/content/13/6/700}, eprint = {https://dmd.aspetjournals.org/content/13/6/700.full.pdf}, journal = {Drug Metabolism and Disposition} }